The goal of the project is to design new macromolecular structures, whose assembly into hybrid hydrogels will be modulated by association of coiled-coil peptide domains. N-(2-hydroxypropyl)rnethacrylamide (HPMA) copolymers containing coiled-coil domains as side-chains (grafts) will be synthesized by copolymerization of HPMA with macromonomers containing coiled-coils. The design of coiled-coil grafts imposes an antiparallel heterodimer formation in the self-assembly process. We hypothesize that the antiparallel orientation of heterodimers will contribute to the homogeneity of the self-assembled hybrid hydrogels due to the unique interchain dimer formation and decreased steric hindrance of the polymer backbone on the "in-register" alignment of heterodimers. Materials with tailor-made structures at the nanometer range will result from the proposed research. A theoretical model will be developed to assist in a rational design of the hybrid hydrogels. Experimental results will be analyzed using the model to provide feedback for the optimization of graft copolymer structure and of the self-assembly into hybrid hydrogels. The self-assembly of HPMA graft copolymers in the presence of encapsulated molecules will be evaluated in an attempt to develop new in-situ forming hybrid hydrogels for the delivery of proteins. The delivery system is suitable for a wide variety of biological molecules since the self-assembly occurs in aqueous media. The new hydrogels may find wide-ranging biomedical applications in drug delivery, biosensors, affinity separations, and nanoreactors. In addition, the possibility to join non-compatible materials, such as hydrophobic muscle mimics from liquid crystalline polymers and hydrogels, may open a new field of research.